Submolecular cooperativity produces multi-state protein unfolding and refolding

S. Walter Englander; Leland Mayne; Jon N. Rumbley

doi:10.1016/S0301-4622(02)00190-4

Submolecular cooperativity produces multi-state protein unfolding and refolding

S. Walter Englander, Leland Mayne, Jon N. Rumbley

Duluth Pharmacy Program

Research output: Contribution to journal › Article › peer-review

38 Scopus citations

Abstract

Hydrogen exchange experiments show that cytochrome c and other proteins under native conditions reversibly unfold in a multi-step manner. The step from one intermediate to the next is determined by the intrinsically cooperative nature of secondary structural elements, which is retained in the native protein. Folding uses the same pathway in the reverse direction, moving from the unfolded to the native state through relatively discrete intermediate forms by the sequential addition of native-like secondary structural units.

Original language	English (US)
Pages (from-to)	57-65
Number of pages	9
Journal	Biophysical Chemistry
Volume	101-102
DOIs	https://doi.org/10.1016/S0301-4622(02)00190-4
State	Published - Dec 10 2002

Bibliographical note

Funding Information:
This work was supported by research grants from the National Institutes of Health and the Mathers Charitable Foundation.

Keywords

Hydrogen exchange
Protein cooperativity
Protein folding
Protein unfolding

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title = "Submolecular cooperativity produces multi-state protein unfolding and refolding",

abstract = "Hydrogen exchange experiments show that cytochrome c and other proteins under native conditions reversibly unfold in a multi-step manner. The step from one intermediate to the next is determined by the intrinsically cooperative nature of secondary structural elements, which is retained in the native protein. Folding uses the same pathway in the reverse direction, moving from the unfolded to the native state through relatively discrete intermediate forms by the sequential addition of native-like secondary structural units.",

keywords = "Hydrogen exchange, Protein cooperativity, Protein folding, Protein unfolding",

author = "Englander, {S. Walter} and Leland Mayne and Rumbley, {Jon N.}",

note = "Funding Information: This work was supported by research grants from the National Institutes of Health and the Mathers Charitable Foundation.",

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doi = "10.1016/S0301-4622(02)00190-4",

language = "English (US)",

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AU - Englander, S. Walter

AU - Mayne, Leland

AU - Rumbley, Jon N.

N1 - Funding Information: This work was supported by research grants from the National Institutes of Health and the Mathers Charitable Foundation.

PY - 2002/12/10

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N2 - Hydrogen exchange experiments show that cytochrome c and other proteins under native conditions reversibly unfold in a multi-step manner. The step from one intermediate to the next is determined by the intrinsically cooperative nature of secondary structural elements, which is retained in the native protein. Folding uses the same pathway in the reverse direction, moving from the unfolded to the native state through relatively discrete intermediate forms by the sequential addition of native-like secondary structural units.

AB - Hydrogen exchange experiments show that cytochrome c and other proteins under native conditions reversibly unfold in a multi-step manner. The step from one intermediate to the next is determined by the intrinsically cooperative nature of secondary structural elements, which is retained in the native protein. Folding uses the same pathway in the reverse direction, moving from the unfolded to the native state through relatively discrete intermediate forms by the sequential addition of native-like secondary structural units.

KW - Hydrogen exchange

KW - Protein cooperativity

KW - Protein folding

KW - Protein unfolding

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JO - Biophysical Chemistry

JF - Biophysical Chemistry

ER -

Submolecular cooperativity produces multi-state protein unfolding and refolding

Abstract

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Keywords

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